Intermolecular disulfide bond formation in the NEMO dimer requires Cys54 and Cys347 (Q24647995)

2

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Thomas Ennis

3

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Kate Coleman

4

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Sheila Yong

5

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Brinda Armstead

6

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Demetrios Kalaitzidis

7

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Sushil Chandani

8

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Thomas D Gilmore

Biochemical and Biophysical Research Communications

9

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language of work or name

English

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publication date

29 February 2008

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published in

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volume

367

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issue

1

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page(s)

103-8

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cites work

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NEMO oligomerization in the dynamic assembly of the IkappaB kinase core complex

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Phosphorylation of serine 68 in the IkappaB kinase (IKK)-binding domain of NEMO interferes with the structure of the IKK complex and tumor necrosis factor-alpha-induced NF-kappaB activity

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A point mutation in NEMO associated with anhidrotic ectodermal dysplasia with immunodeficiency pathology results in destabilization of the oligomer and reduces lipopolysaccharide- and tumor necrosis factor-mediated NF-kappa B activation

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The trimerization domain of NEMO is composed of the interacting C-terminal CC2 and LZ coiled-coil subdomains

28 September 2017

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Immortalized embryonic mouse fibroblasts lacking the RelA subunit of transcription factor NF-kappaB have a malignantly transformed phenotype

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Cytokine-induced activation of nuclear factor-kappa B is inhibited by hydrogen peroxide through oxidative inactivation of IkappaB kinase

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IKKgamma /NEMO facilitates the recruitment of the IkappaB proteins into the IkappaB kinase complex

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